2i08: Difference between revisions
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<StructureSection load='2i08' size='340' side='right' caption='[[2i08]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2i08' size='340' side='right' caption='[[2i08]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2i08]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2i08]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I08 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2I08 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">calm1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">calm1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i08 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2i08 RCSB], [http://www.ebi.ac.uk/pdbsum/2i08 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i08 OCA], [http://pdbe.org/2i08 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2i08 RCSB], [http://www.ebi.ac.uk/pdbsum/2i08 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Human]] | ||
[[Category: Ababou, A]] | [[Category: Ababou, A]] | ||
[[Category: Desjarlais, J R]] | [[Category: Desjarlais, J R]] | ||
Revision as of 13:34, 11 September 2015
Solvation effect in conformational changes of EF-hand proteins: X-ray structure of Ca2+-saturated double mutant Q41L-K75I of N-domain of calmodulinSolvation effect in conformational changes of EF-hand proteins: X-ray structure of Ca2+-saturated double mutant Q41L-K75I of N-domain of calmodulin
Structural highlights
Function[CALM_XENLA] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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